PrP 106-126
(Synonyms: Prion protein (106-126)) 目录号 : GC34261
PrP(106-126)是与朊病毒蛋白的淀粉样区域相对应的多肽段，它的生化特性类似于朊病毒蛋白的感染区域。
Cas No.:148439-49-0
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Cell experiment: | The toxicity of PrP peptides is investigated on monolayers of PBEC. 100 000 PBEC/cm2 are seeded on 96 [for 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT)] or 24-well plates [for lactate dehydrogenase (LDH)] pre-coated with rat tail collagen (27 μg/mL). The cell monolayers are treated with either PrP 106-126 wt or scr peptides. The PrP peptides are dissolved in double distilled water and then diluted in assay medium or in 5% newborn calf serum in Dulbecco-modified Earl's medium without phenol red. Treatment duration with the PrP peptides varies from 24 h to 48 h and the peptide concentration is set to 100 μM at which it exerts optimal effects as shown in a dose-dependent experiment. This concentration is also chosen as similar concentrations of PrP 106-126 found to exert in-vitro effects on astrocytes, neurons, microglia and leukocytes. The MTT assay, which measures mitochondrial metabolism, is based on the conversion of the water-soluble MTT dye [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] to an insoluble purple formazan. This formazan is then solubilized in pure dimethylsulfoxide, and its concentration determined by optical density (550/630 nm). The LDH cell death assay is done using the CytoTox 96® Assay kit. The released LDH in culture supernatants is measured with a 30-min coupled enzymatic assay which results in the conversion of a tetrazolium salt, 2-p-iodophenyl-3-p-nitro-phenyl-5-phenyl tetrazolium chloride (INT) into a red formazan product. The LDH levels are measured at the end of each treatment period. Thus, 50 μL of the medium is removed at the end of the treatment with PrP peptides and transferred to a new 96-well plate to which the other compounds are added. The plates are analyzed using an Elisa reader with the 490 nm filter. |
References: [1]. Yang W, et al. PRAS40 alleviates neurotoxic prion peptide-induced apoptosis via mTOR-AKT signaling. CNS Neurosci Ther. 2017 May;23(5):416-427. | |
PrP (106-126) is a peptide corresponding to the prion protein (PrP) amyloidogenic region, and its biochemical properties resemble the infectious form of prion protein.
PrP (106-126) (100 μM) induces mTOR phosphorylation over time in N2a cells. PrP (106-126)-treated cells show significantly increased ROS production in comparison with that of PBS-treated control cells. Knockdown of PRAS40 enhances PrP (106-126)-induced apoptosis. PRAS40 alleviates PrP (106-126)-induced neuronal apoptosis via mTOR-AKT activation[1]. PrP (106-126) interacts selectively with porcine brain endothelial cells (PBEC) via their luminal side, and causes cumulative cell death, as shown by lactate dehydrogenase release, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide reduction, Caspase 3 induction and direct cell counting. In addition, PrP (106-126), but not its corresponding scrambled peptide, produces a 50% reduction of the trans-endothelial electrical resistance, while the PBEC maintained confluency[2].
[1]. Yang W, et al. PRAS40 alleviates neurotoxic prion peptide-induced apoptosis via mTOR-AKT signaling. CNS Neurosci Ther. 2017 May;23(5):416-427. [2]. Cooper I, et al. Interactions of the prion peptide (PrP 106-126) with brain capillary endothelial cells: coordinated cell killing and remodeling of intercellular junctions. J Neurochem. 2011 Feb;116(4):467-75.
| Cas No. | 148439-49-0 | SDF | |
| 别名 | Prion protein (106-126) | ||
| Canonical SMILES | Lys-Thr-Asn-Met-Lys-His-Met-Ala-Gly-Ala-Ala-Ala-Ala-Gly-Ala-Val-Val-Gly-Gly-Leu-Gly | ||
| 分子式 | C80H138N26O24S2 | 分子量 | 1912.3 |
| 溶解度 | Water : 1 mg/mL (0.52 mM) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.5229 mL | 2.6147 mL | 5.2293 mL |
| 5 mM | 0.1046 mL | 0.5229 mL | 1.0459 mL |
| 10 mM | 0.0523 mL | 0.2615 mL | 0.5229 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
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| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
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Review: PrP 106-126 - 25 years after
Neuropathol Appl Neurobiol 2019 Aug;45(5):430-440.PMID:30635947DOI:10.1111/nan.12538.
A quarter of a century ago, we proposed an innovative approach to study the pathogenesis of prion disease, one of the most intriguing biomedical problems that remains unresolved. The synthesis of a peptide homologous to residues 106-126 of the human prion protein (PrP106-126), a sequence present in the PrP amyloid protein of Gerstmann-Sträussler-Scheinker syndrome patients, provided a tractable tool for investigating the mechanisms of neurotoxicity. Together with several other discoveries at the beginning of the 1990s, PrP106-126 contributed to underpin the role of amyloid in the pathogenesis of protein-misfolding neurodegenerative disorders. Later, the role of oligomers on one hand and of prion-like spreading of pathology on the other further clarified mechanisms shared by different neurodegenerative conditions. Our original report on PrP106-126 neurotoxicity also highlighted a role for programmed cell death in CNS diseases. In this review, we analyse the prion research context in which PrP106-126 first appeared and the advances in our understanding of prion disease pathogenesis and therapeutic perspectives 25 years later.
PrP 106-126 altered PrP mRNA gene expression in mouse microglia BV-2 cells
Virol Sin 2010 Dec;25(6):440-4.PMID:21221923DOI:10.1007/s12250-010-3143-z.
Prion diseases are infectious and fatal neurodegenerative diseases. The pathogenic agent is an abnormal prion protein aggregate. Microglial activation in the centre nervous system is a characteristic feature of prion disease. In this study, we examined the effect of PrP 106-126 on PrP mRNA gene expression in Mouse microglia cells BV-2 by real-time quantitative PCR. PrP mRNA expression level was found to be significantly increased after 18 h exposure of BV-2 cells to PrP 106-126, with 3-fold increase after 18 h and 4.5-fold increase after 24 h and BV-2 cells proliferating occurred correspondingly. Our results provide the first in vitro evidence of the increase of PrP mRNA levels in microglial cells exposed to PrP 106-126, and indicate that microglial cells might play a critical role in prion pathogenesis.
Acetylcholinesterase triggers the aggregation of PrP 106-126
Biochem Biophys Res Commun 2006 Jul 21;346(1):89-94.PMID:16750169DOI:10.1016/j.bbrc.2006.04.187.
Acetylcholinesterase (AChE), a senile plaque component, promotes amyloid-beta-protein (Abeta) fibril formation in vitro. The presence of prion protein (PrP) in Alzheimer's disease (AD) senile plaques prompted us to assess if AChE could trigger the PrP peptides aggregation as well. Consequently, the efficacy of AChE on the PrP peptide spanning-residues 106-126 aggregation containing a coumarin fluorescence probe (coumarin-PrP 106-126) was studied. Kinetics of coumarin-PrP 106-126 aggregation showed a significant increase of maximum size of aggregates (MSA), which was dependent on AChE concentration. AChE-PrP 106-126 aggregates showed the tinctorial and optical amyloid properties as determined by polarized light and electronic microscopy analysis. A remarkable inhibition of MSA was obtained with propidium iodide, suggesting that AChE triggers PrP 106-126 and Abeta aggregation through a similar mechanism. Huprines (AChE inhibitors) also significantly decreased MSA induced by AChE as well, unveiling the potential interest for some AChE inhibitors as a novel class of potential anti-prion drugs.
In vitro effect of prion peptide PrP 106-126 on mouse macrophages: Possible role of macrophages in transport and proliferation for prion protein
Microb Pathog 2008 Feb;44(2):129-34.PMID:17904794DOI:10.1016/j.micpath.2007.08.014.
While there is a growing consensus on the understanding that the immune system plays an important role in facilitating the spread of prion infections from the periphery to the central nervous system, little is known about the key players in the first steps of the infection and about the sites of the disease development. Owing to their subepithelial location and their migratory capacity, macrophages could be early targets for prion transportation or propagation during the later stages of disease. In order to investigate the role of macrophages, we studied in vitro the effect of exposing primary peritoneal macrophages to a synthetic peptide homologous to residues 106-126 of the human prion protein (PrP), PrP 106-126. As shown by MTT assay, macrophage viability treated with less than 50 microM PrP 106-126 for 72 h was not inhibited but slightly stimulated at 10 and 25 microM, while there was significant decrease when exposed to 100 microM PrP 106-126 for 72 h. The expressions of PrP at mRNA and protein level were up-regulated following treatment with PrP 106-126 for 72 h. Cytokine TNF-alpha production were elevated by the PrP peptide in a time-dependent manner, which demonstrated a proinflammatory response linked to the presence and progression of prion disease took place in macrophages. These findings suggested that macrophages may play roles in the transportation and replication of the infectious agent.
Interactions of the prion peptide (PrP 106-126) with brain capillary endothelial cells: coordinated cell killing and remodeling of intercellular junctions
J Neurochem 2011 Feb;116(4):467-75.PMID:20804519DOI:10.1111/j.1471-4159.2010.06934.x.
We studied here the interactions of PrP 106-126, a peptide corresponding to the prion protein (PrP) amyloidogenic region, with a blood-brain barrier in vitro model consisting of confluent porcine brain endothelial cells (PBEC). PrP 106-126 interacted selectively with PBEC via their luminal side, and caused cumulative cell death, as shown by lactate dehydrogenase release, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide reduction, Caspase 3 induction and direct cell counting. In addition, PrP 106-126, but not its corresponding scrambled peptide, produced a 50% reduction of the trans-endothelial electrical resistance, while the PBEC maintained confluency. This process was accompanied by a 23% increase of PBEC average size and the selective disappearance from the cell borders of the junction proteins occludin, claudin-5 and VE-cadherin (but not ZO-1), as evaluated by immunostaining. These results fit with a mechanism by which PrP 106-126 initiates a coordinated cell killing process ultimately causing the remaining cells to undergo a coordinated remodeling of the intercellular junctions and an expansion of their cell territory.